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P22811 (XDH_DROPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xanthine dehydrogenase
Short name=XD
EC=1.17.1.4
Alternative name(s):
Protein rosy locus
Gene names
Name:ry
Synonyms:XDH
ORF Names:GA20500
OrganismDrosophila pseudoobscura pseudoobscura (Fruit fly) [Reference proteome]
Taxonomic identifier46245 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length1343 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid By similarity.

Catalytic activity

Xanthine + NAD+ + H2O = urate + NADH.

Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Cofactor

Binds 2 2Fe-2S clusters By similarity.

FAD By similarity.

Binds 1 molybdenum ion (molybdopterin) per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 FAD-binding PCMH-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13431343Xanthine dehydrogenase
PRO_0000166080

Regions

Domain8 – 95882Fe-2S ferredoxin-type
Domain235 – 424190FAD-binding PCMH-type
Nucleotide binding263 – 2708FAD By similarity
Nucleotide binding353 – 3575FAD By similarity

Sites

Active site12751Proton acceptor By similarity
Metal binding471Iron-sulfur 1 By similarity
Metal binding521Iron-sulfur 1 By similarity
Metal binding551Iron-sulfur 1 By similarity
Metal binding771Iron-sulfur 1 By similarity
Metal binding1171Iron-sulfur 2 By similarity
Metal binding1201Iron-sulfur 2 By similarity
Metal binding1521Iron-sulfur 2 By similarity
Metal binding1541Iron-sulfur 2 By similarity
Metal binding7801Molybdenum By similarity
Metal binding8111Molybdenum; via carbonyl oxygen By similarity
Metal binding9251Molybdenum; via amide nitrogen By similarity
Metal binding10921Molybdenum; via amide nitrogen By similarity
Binding site3431FAD By similarity
Binding site3661FAD By similarity
Binding site4141FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site4321FAD By similarity
Binding site8151Substrate By similarity
Binding site8931Substrate By similarity
Binding site9271Substrate By similarity

Experimental info

Sequence conflict581V → M in AAA29022. Ref.1
Sequence conflict2001T → A in AAA29022. Ref.1
Sequence conflict4281V → I in AAA29022. Ref.1
Sequence conflict4281V → I in AAX13180. Ref.3
Sequence conflict4611G → E in AAA29022. Ref.1
Sequence conflict4611G → E in AAX13180. Ref.3
Sequence conflict4751L → V in AAA29022. Ref.1
Sequence conflict7341E → D in AAX13180. Ref.3
Sequence conflict7471S → N in AAA29022. Ref.1
Sequence conflict7621A → G in AAA29022. Ref.1
Sequence conflict9861A → V in AAX13180. Ref.3
Sequence conflict12451Missing in AAA29022. Ref.1
Sequence conflict13201C → F in AAA29022. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P22811 [UniParc].

Last modified July 11, 2006. Version 2.
Checksum: A58C142336E14BC9

FASTA1,343147,349
        10         20         30         40         50         60 
MSGQQKTSEL VFFVNGKKVT DTNPDPECTL LTYLRDKLRL CGTKLGCAEG GCGACTVVIS 

        70         80         90        100        110        120 
RMDRGQNKIR HLAVNACLTP VCAMHGCAVT TVEGIGSTRT RLHPVQERLA KAHGSQCGFC 

       130        140        150        160        170        180 
TPGIVMSMYA LLRSAEQPSM RDLEVAFQGN LCRCTGYRPI LEGYKTFTKE FACGMGDKCC 

       190        200        210        220        230        240 
KVNGKGCGGG DDTQSVTDDT LFERSQFQPL DPSQEPIFPP ELQLTPTYDS ESLIFSSERV 

       250        260        270        280        290        300 
TWYRPTTLQE LLQLKSDHPS AKLVVGNTEV GVEVKFKHFL YPHLINPTQV PELLEVRESE 

       310        320        330        340        350        360 
ESIYFGAAVS LMEIDALLRQ RIEELPEAQT RLFQCAVDML HYFAGKQIRN VACLGGNIMT 

       370        380        390        400        410        420 
GSPISDMNPV LTAAGARLEV ASLVGGKTSH RTVHMGTGFF TGYRRNVIEP HEVLLGIHFQ 

       430        440        450        460        470        480 
KTTPDQHVVA FKQARRRDDD IAIVNAAVNV RFEPRTNVVA GISMAFGGMA PTTVLAPRTS 

       490        500        510        520        530        540 
QLMVKQPLDH HLVERVAESL CGELPLAASA PGGMIAYRRA LVVSLIFKAY LSISRKLSEA 

       550        560        570        580        590        600 
GIISTDAIPA EERSGAELFH TPVLRSAQLF ERVCSEQPVC DPIGRPEVHA AALKQATGEA 

       610        620        630        640        650        660 
IYTDDIPRMD GELYLGLVLS TKPRAKITKL DASEALALEG VHAFFSHKDL TEHENEVGPV 

       670        680        690        700        710        720 
FHDEHVFAAA EVHCYGQIVG AVAADNKALA QRAARLVRVE YEELAPVIVT IEQAIEHGSY 

       730        740        750        760        770        780 
FPDYPRYVNK GNVEEAFAAA EHTYEGSCRM GGQEHFYLET HAAVAVPRDS DELELFCSTQ 

       790        800        810        820        830        840 
HPSEVQKLVA HVTTLPAHRV VCRAKRLGGG FGGKESRGIS VALPVALAAY RLRRPVRCML 

       850        860        870        880        890        900 
DRDEDMLITG TRHPFLFKYK VAFASDGLIT ACDIECYNNA GWSMDLSFSV LERAMYHFEN 

       910        920        930        940        950        960 
CYRIPNVRVG GWVCKTNLPS NTAFRGFGGP QGMFAGEHII RDVARIVGRD VLDVMRLNFY 

       970        980        990       1000       1010       1020 
KTGDITHYNQ KLEHFPIERC LDDCLAQSRY HEKRTEIAKF NRENRWRKRG MAVIPTKYGI 

      1030       1040       1050       1060       1070       1080 
AFGVMHLNQA GALINVYGDG SVLLSHGGVE IGQGLNTKMI QCAARALGIP IELIHISETA 

      1090       1100       1110       1120       1130       1140 
TDKVPNTSPT AASVGSDLNG MAVLDACEKL NKRLAPIKEA LPQGTWQEWI NKAYFDRVSL 

      1150       1160       1170       1180       1190       1200 
SATGFYAMPG IGYHPETNPN ARTYSYYTNG VGISVVEIDC LTGDHQVLST DIVMDIGSSI 

      1210       1220       1230       1240       1250       1260 
NPAIDIGQIE GAFMQGYGLF TLEELMYSPQ GMLYSRGPGM YKLPGFADIP GEFNVSLLTG 

      1270       1280       1290       1300       1310       1320 
APNPRAVYSS KAVGEPPLFI GSSAFFAIKE AIAAARQEQG LTGDFPLEAP STSARIRMAC 

      1330       1340 
QDKFTNLLEI PEEGSFTPWN IVP

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Xdh region in Drosophila pseudoobscura and an analysis of the evolution of synonymous codons."
Riley M.A.
Mol. Biol. Evol. 6:33-52(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution."
Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F., Howells S.L. expand/collapse author list , Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., Weinstock G.M., Gibbs R.A.
Genome Res. 15:1-18(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MV2-25 / Tucson 14011-0121.94.
[3]"Patterns of selection on synonymous and nonsynonymous variants in Drosophila miranda."
Bartolome C., Maside X., Yi S., Grant A.L., Charlesworth B.
Genetics 169:1495-1507(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-1062.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M33977 Genomic DNA. Translation: AAA29022.1.
CM000070 Genomic DNA. Translation: EAL27642.2.
AY754605 Genomic DNA. Translation: AAX13180.1.
PIRA31946.
RefSeqXP_001358503.2. XM_001358466.2.

3D structure databases

ProteinModelPortalP22811.
SMRP22811. Positions 9-169.
ModBaseSearch...

Protein-protein interaction databases

STRING7237.FBpp0282224.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0283786; FBpp0282224; FBgn0012736.
GeneID4801405.
KEGGdpo:Dpse_GA20500.

Organism-specific databases

FlyBaseFBgn0012736. Dpse\ry.

Phylogenomic databases

eggNOGCOG4630.
InParanoidP22811.
KOK00106.
OrthoDBEOG418937.

Family and domain databases

Gene3D1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFPIRSF000127. Xanthine_DH. 1 hit.
SMARTSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF47741. 2Fe-2S_bind. 1 hit.
SSF56003. Ald_xan_DH_mo_bd. 1 hit.
SSF54665. Aldxan_dh_hamm. 1 hit.
SSF55447. CO_deh_flav_C. 1 hit.
SSF56176. FAD-binding_2. 1 hit.
SSF54292. Ferredoxin. 1 hit.
TIGRFAMsTIGR02963. xanthine_xdhA. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXDH_DROPS
AccessionPrimary (citable) accession number: P22811
Secondary accession number(s): Q299Q9, Q56RA2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 11, 2006
Last modified: May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents